4RHV

THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT OF THE HUMAN RHINOVIRUS 14 STRUCTURE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Work: 0.160 

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This is version 2.1 of the entry. See complete history


Literature

The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure.

Arnold, E.Rossmann, M.G.

(1988) Acta Crystallogr A 44: 270-282

  • DOI: https://doi.org/10.1107/s0108767387011875
  • Primary Citation of Related Structures:  
    4RHV

  • PubMed Abstract: 

    The structure of human rhinovirus 14 has been refined, by the method of restrained least squares, to an R factor of 0.16 for various random samples between 6 and 3 A resolution with F greater than 3 sigma (F). As a first step the non-crystallographic symmetry parameters were optimized using the initial atomic model in a rigid-body refinement procedure. Phase determination by the molecular-replacement phase extension and refinement procedure was continued to 2.94 A resolution, employing the improved non-crystallographic symmetry operators. The resultant structure-factor phases and weights, together with the measured amplitudes, constituted the X-ray observations used in the restrained refinement. The Hendrickson-Konnert program system [Konnert & Hendrickson (1980). Acta Cryst. A36, 344-350] was modified to incorporate non-crystallographic symmetry constrains and structure-factor phases as observations. The non-bonded contacts between subunits related by non-crystallographic symmetry were also restrained.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, West Lafayette, Indiania 47907.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1)A [auth 1]289rhinovirus B14Mutation(s): 0 
UniProt
Find proteins for P03303 (Human rhinovirus 14)
Explore P03303 
Go to UniProtKB:  P03303
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03303
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2)B [auth 2]262rhinovirus B14Mutation(s): 0 
UniProt
Find proteins for P03303 (Human rhinovirus 14)
Explore P03303 
Go to UniProtKB:  P03303
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03303
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3)C [auth 3]236rhinovirus B14Mutation(s): 0 
UniProt
Find proteins for P03303 (Human rhinovirus 14)
Explore P03303 
Go to UniProtKB:  P03303
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03303
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP4)D [auth 4]68rhinovirus B14Mutation(s): 0 
UniProt
Find proteins for P03303 (Human rhinovirus 14)
Explore P03303 
Go to UniProtKB:  P03303
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03303
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Work: 0.160 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 445.1α = 90
b = 445.1β = 90
c = 445.1γ = 90

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1988-04-16
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2023-01-18
    Type: Remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Other, Refinement description
  • Version 2.1: 2024-05-22
    Changes: Data collection